1dbp
From Proteopedia
(Difference between revisions)
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<StructureSection load='1dbp' size='340' side='right'caption='[[1dbp]], [[Resolution|resolution]] 2.20Å' scene=''> | <StructureSection load='1dbp' size='340' side='right'caption='[[1dbp]], [[Resolution|resolution]] 2.20Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1dbp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <table><tr><td colspan='2'>[[1dbp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DBP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DBP FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RIP:RIBOSE(PYRANOSE+FORM)'>RIP</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=RIP:RIBOSE(PYRANOSE+FORM)'>RIP</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dbp OCA], [https://pdbe.org/1dbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dbp RCSB], [https://www.ebi.ac.uk/pdbsum/1dbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dbp ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1dbp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dbp OCA], [https://pdbe.org/1dbp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dbp RCSB], [https://www.ebi.ac.uk/pdbsum/1dbp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dbp ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/RBSB_ECOLI RBSB_ECOLI] Involved in the high-affinity D-ribose membrane transport system and also serves as the primary chemoreceptor for chemotaxis. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dbp ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1dbp ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | The x-ray structure of a mutant (Gly72 to Asp) of the Escherichia coli ribose-binding protein with altered transport function has been solved and refined to 2.2-A resolution with a conventional R-factor (R-factor = [formula: see text]) of 16.0% and good stereochemistry. Comparison with the wild type ribose-binding protein shows that the structure is disturbed little at the actual mutation site, but quite appreciably in a neighboring loop. Changes in the surface of the protein at the site of mutation, however, seem to explain the functional effects. A corresponding mutation of the related glucose/galactose-binding protein has different structural and functional effects due to the different structural context of the mutation site in that protein. These results are consistent with the concept that these proteins have slightly different ways of interacting with the membrane components in transport and chemotaxis. | ||
| - | |||
| - | Identical mutations at corresponding positions in two homologous proteins with nonidentical effects.,Bjorkman AJ, Binnie RA, Cole LB, Zhang H, Hermodson MA, Mowbray SL J Biol Chem. 1994 Apr 15;269(15):11196-200. PMID:8157648<ref>PMID:8157648</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1dbp" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Ribose-binding protein|Ribose-binding protein]] | *[[Ribose-binding protein|Ribose-binding protein]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Bjorkman | + | [[Category: Joakim Bjorkman AJ]] |
| - | [[Category: Mowbray | + | [[Category: Mowbray SL]] |
| - | + | ||
Current revision
IDENTICAL MUTATIONS AT CORRESPONDING POSITIONS IN TWO HOMOLOGOUS PROTEINS WITH NON-IDENTICAL EFFECTS
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